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The major glycoprotein component of animal cell basement membranes, laminin, is involved in a variety of cellular activities, including cell adhesion, differentiation, and mitogenesis, that are mediated by the interaction of laminin with specific cell-surface receptors. A laminin-binding protein with an apparent molecular mass of 68 to 72 kD was first characterized in mammalian tumor cells and considered as “the laminin receptor” (Liotta et al., 1986; Wewer et al., 1986). Severa1 putative cDNA clones encoding this protein have been isolated from mammals (Yow et al., 1988; Rao et al., 1989; Van den Ouweland et al., 1989; Grosso et al., 1991). A11 the clones contained an open reading frame coding for a highly conserved polypeptide with a calculated molecular mass of 33 kD. Independently, a cDNA encoding an identical polypeptide was isolated from mouse tumor cells (Makrides et al., 1988), but the expressed protein, named factor p40, was shown to be a component of the translation machinery (Auth and Brawerman, 1992). Recently, DNA-deduced amino acid sequences exhibiting homology with the previously characterized 33-kD ”laminin receptor” were identified from hydra (Keppel and Schaller, 1991), Drosophila (M.B. Melnick, T.B. Chou, and N. Perrimon, accession No. M90422), and yeast (J. Miles and T.G. Formosa, accession No. M88277). We have isolated a cDNA clone (At lrhl) from a cDNA library of Arabidopsis thaliana cultured cells showing a striking homology to the laminin receptor cDNAs (Table I). Nucleotide homology of Atlrhl with the above-mentioned DNA sequences was restricted to the first two-thirds of the coding sequence, with highest homology to the human cDNA (66% identity). In the same way, the Atlrhl deduced polypeptide, 298 residues long, showed strong homology with the deduced protein sequences of other species from amino acids 12 to 222. In this region, mouse, human, and Drosophila polypeptides showed the highest homology to the plant sequence, corresponding to 60 to 62% identity and 78 to 79% similarity accounting for the conservative substitutions. No significant homology was found in the carboxy-terminal region from amino acids 223 to 298, apart from a relatively high conserved content in Trp. It is an intriguing feature that a11

An Arabidopsis cDNA Encoding a 33-Kilodalton Laminin Receptor Homolog